Preparation, characterization and anticancer applications of HAase from Pedobacter heparinus.

Authors

Bo Dou, Ruiqi Wu, Xiaolai Ma, Changhua Hu, Xiaoqun Duan

Published in

BMC cancer. Jun 26, 2026. Epub Jun 26, 2026.

Abstract

Hyaluronidase (HAase) is an enzyme capable of degrading hyaluronic acid (HA). In anti-tumor therapy, HAase can enhance the efficacy of anti-cancer drugs by regulating the tumor microenvironment and overcoming drug delivery barriers, and it can also be used directly to inhibit tumor growth. In this study, we identified a previously uncharacterized HAase (Ph-HAase) from Pedobacter heparinus. After purification, the enzyme was obtained with a 43.08% recovery, a 47.5-fold purification, and a specific activity of 32.32 IU/mg. SDS-PAGE and LC-MS analyses revealed that the molecular weight of Ph-HAase was 79.6 kDa. Ph-HAase exhibited excellent stability at temperatures below 30 °C and within the pH range of 6.5 to 7.5. The enzyme activity was found to be relatively high at pH 6.5 and 45℃. Although HA served as the preferred substrate, Ph-HAase also exhibited degradative activity toward Chondroitin Sulfate (CS) and Dermatan Sulfate (DS). Notably, we found that Ph-HAase induced apoptosis in melanoma B16F10 cells via the mitochondrial pathway, characterized by loss of membrane potential and ROS accumulation, and affected the expression of apoptosis-related genes and proteins. In vivo studies further confirmed its anti-melanoma effect. This study is the first to report HAase derived from P. heparinus and to demonstrate its potential for melanoma treatment.

PMID:
42363124
Bibliographic data and abstract were imported from PubMed on 27 Jun 2026.

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